ID M7BE58_CHEMY Unreviewed; 1299 AA.
AC M7BE58;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE SubName: Full=Proprotein convertase subtilisin/kexin type 5 {ECO:0000313|EMBL:EMP30423.1};
GN ORFNames=UY3_12424 {ECO:0000313|EMBL:EMP30423.1};
OS Chelonia mydas (Green sea-turtle) (Chelonia agassizi).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira;
OC Americhelydia; Chelonioidea; Cheloniidae; Chelonia.
OX NCBI_TaxID=8469 {ECO:0000313|EMBL:EMP30423.1, ECO:0000313|Proteomes:UP000031443};
RN [1] {ECO:0000313|Proteomes:UP000031443}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23624526; DOI=10.1038/ng.2615;
RA Wang Z., Pascual-Anaya J., Zadissa A., Li W., Niimura Y., Huang Z., Li C.,
RA White S., Xiong Z., Fang D., Wang B., Ming Y., Chen Y., Zheng Y.,
RA Kuraku S., Pignatelli M., Herrero J., Beal K., Nozawa M., Li Q., Wang J.,
RA Zhang H., Yu L., Shigenobu S., Wang J., Liu J., Flicek P., Searle S.,
RA Wang J., Kuratani S., Yin Y., Aken B., Zhang G., Irie N.;
RT "The draft genomes of soft-shell turtle and green sea turtle yield insights
RT into the development and evolution of the turtle-specific body plan.";
RL Nat. Genet. 45:701-706(2013).
CC -!- SIMILARITY: Belongs to the peptidase S8 family.
CC {ECO:0000256|ARBA:ARBA00011073, ECO:0000256|PROSITE-ProRule:PRU01240}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU01240}.
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DR EMBL; KB549795; EMP30423.1; -; Genomic_DNA.
DR STRING; 8469.M7BE58; -.
DR Proteomes; UP000031443; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00064; FU; 12.
DR CDD; cd04059; Peptidases_S8_Protein_convertases_Kexins_Furin-like; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR006212; Furin_repeat.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR032778; GF_recep_IV.
DR InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR InterPro; IPR034182; Kexin/furin.
DR InterPro; IPR002884; P_dom.
DR InterPro; IPR000209; Peptidase_S8/S53_dom.
DR InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR PANTHER; PTHR42884; PROPROTEIN CONVERTASE SUBTILISIN/KEXIN-RELATED; 1.
DR PANTHER; PTHR42884:SF7; PROPROTEIN CONVERTASE SUBTILISIN_KEXIN TYPE 5; 1.
DR Pfam; PF14843; GF_recep_IV; 1.
DR Pfam; PF01483; P_proprotein; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR SMART; SM00181; EGF; 7.
DR SMART; SM01411; Ephrin_rec_like; 5.
DR SMART; SM00261; FU; 12.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR SUPFAM; SSF57184; Growth factor receptor domain; 6.
DR SUPFAM; SSF52743; Subtilisin-like; 1.
DR PROSITE; PS51829; P_HOMO_B; 1.
DR PROSITE; PS51892; SUBTILASE; 1.
DR PROSITE; PS00138; SUBTILASE_SER; 1.
PE 3: Inferred from homology;
KW Cleavage on pair of basic residues {ECO:0000256|ARBA:ARBA00022685};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000031443};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT TRANSMEM 1183..1203
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 188..339
FT /note="P/Homo B"
FT /evidence="ECO:0000259|PROSITE:PS51829"
FT REGION 345..365
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1228..1264
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 347..361
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1228..1248
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1249..1264
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1299 AA; 144031 MW; 7E676B4E29B00A28 CRC64;
MLDGDVTDMV EAKSLSLNPQ HIHIYSASWG PDDDGKTVDG PASLARQAFE NGIRTGRNKL
GSIFVWASGN GGRSKDHCSC DGYTNSIYTI SISSTAESGK KPWYLEECAS TLATTYSSGE
SYDKKIITTD LRQRCTDSHT GTSASAPMAA GIIALALEAN PSLTWRDVQH IIVRTSRAGH
LNSNDWKTNA AGYKGDYCED VIINAICKLI FCILRTIRPD SQVHSVYKAT GCSDNSNHHV
IYLEHVVVRI TITHPRRGDL AIFLTSPSGT KSQLLANRLF DHSTEGFKNW EFMTTHCWGE
KAAGDWKLEI HDTPSQLRSF KSPGKLKEWS LVLYGTSIQP YSPRNDFPKV ERVRSSPVED
PTEDYGTDDY AGPCNAECSK VGCDGPGPDH CTDCLHYYYK SKNNTRICVP NCPPGHYNAD
KKRCKKCSPN CETCVGSHSD QCLSCKSGYY LNEESNSCIT SCPDGFYLDK NKIACRKCSE
NCKTCAESQS CTECRHGLSL YGSRCAVRCE EGKYHNGREC EPCHRSCATC AGSGADACIN
CTEGYFMEDG RCVQSCSAGY YLDHSLENGY KTCKRCDASC LECSGQGDKN CTTCPNGYIL
DTGVCVIGTV CKDELNWHNG FDLAGLVKTC SIDGRALCHR FLYSTTMRGG SNVGGRASPI
DIKKCGPCGE YAERVDRCLF CEASCSKCTG PTQNDCIGCA ITRFFDDGQC VLQCPKGKFE
FNNQCHLCHH TCRACSGSEP NKCTACGTDD PRICTACVHN YYMYKQHCYK NCPENTYNDE
STLQCIECDE NCISCDNYEC YWCKKGFYLL DGECVNDCRA GFYSDEDFAE CEECHRTCAT
CDGLNFDDCT SCKQNLQLLH GKCVNPKNMV VEGKFWNDSK KKFQRCDSSC RTCDGADNVC
TSCPEVCMDQ FFLHNGKCLP DCPSGFYADS RSCSPCHEDC RECDGPDSDD CNECASRSFV
LHNGECFGEC PEGTYYETET EDCQVMRDDV SHATAPVRLA MENTTLSAIP ADRAGTNRER
DAYKSVQLDI MQTTPSDCAR DATKAVKSVW DLSPQTVCPV IHIPSCCTPR MNVSPLALNI
IMMIVKQMSV RDATLPAAPA KGDQSECEKC HDTCVECKGP GPLNCTVCPA NMKLYLDEGR
CVKCCDSSNL TETQECCDCS ETQDECVLQT ILNLPAQSKG KTALFVATSI LLILCIGAIA
FIWRRSQAKA QTVNRGGYEK LTDHSKPFSS YKSNHHDSTS YQDDQVTEYK DWDNEDEEED
DDIVYMSQDG TVYRKFKYGL LEDEEEDELE YDDESYSFR
//
